gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Renin binding protein

The gene product inhibits renin activity by forming a dimer with renin, a complex known as high molecular weight renin. The encoded protein contains a leucine zipper domain, which is essential for its dimerization with renin. The gene product can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Transcript variants utilizing alternative promoters have been described in the literature. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: RAGE, CAN, V1a, Serum albumin, HAD
Papers on AGE
A Snapshot of the Plant Glycated Proteome: Structural, Functional and Mechanistic Aspects.
Frolov et al., Germany. In J Biol Chem, Feb 2016
Thus, the knowledge of the plant AGE patterns and the underlying pathways of their formation are completely missing.
High dietary advanced glycation end products are associated with poorer spatial learning and accelerated Aβ deposition in an Alzheimer mouse model.
Schnaider-Beeri et al., Ramat Gan, Israel. In Aging Cell, Feb 2016
We found that AD-like model mice on high-AGE diet due to irradiation had significantly poorer memory, higher hippocampal levels of insoluble Aβ42 and AGEs as well as higher levels of oxidative stress on vascular walls, compared to littermates fed an isocaloric diet.
Damaging effects of hyperglycemia on cardiovascular function: spotlight on glucose metabolic pathways.
Essop et al., Stellenbosch, South Africa. In Am J Physiol Heart Circ Physiol, Feb 2016
In this process the AGE pathway emerges as a crucial mediator of hyperglycemia-mediated detrimental effects.
Glycative stress from advanced glycation end products (AGEs) and dicarbonyls: An emerging biological factor in cancer onset and progression.
Yen et al., T'ai-chung-shih, Taiwan. In Mol Nutr Food Res, Feb 2016
These dicarbonyls not only fuel the AGE pool in living organisms but also evoke carbonyl stress, which may contribute to the carbonylative damage of carbohydrates, lipids, proteins or DNA.
Aged Garlic Extract Modifies Human Immunity.
Percival, Gainesville, United States. In J Nutr, Feb 2016
The purpose of this review was to summarize the influence of aged garlic extract (AGE) on the immune system.
Aged Garlic Extract Inhibits Human Platelet Aggregation by Altering Intracellular Signaling and Platelet Shape Change.
Smith et al., Liverpool, United Kingdom. In J Nutr, Feb 2016
Aged garlic extract (AGE) decreases platelet aggregation; however, the mechanisms involved are not clearly defined.
Garlic and Heart Disease.
Budoff et al., Saskatoon, Canada. In J Nutr, Feb 2016
The most consistent benefits were shown in studies that used aged garlic extract (AGE).
Alagebrium attenuates methylglyoxal induced oxidative stress and AGE formation in H9C2 cardiac myocytes.
Desai et al., Hyderābād, India. In Life Sci, Feb 2016
AIM: Diabetes mellitus associated cardiovascular complications are a leading cause of morbidity and mortality worldwide.
Advanced Glycation End Products: Link between Diet and Ovulatory Dysfunction in PCOS?
Merhi et al., United States. In Nutrients, 2014
Elevation in bodily AGEs, produced endogenously or absorbed exogenously from high-AGE diets, is further exaggerated in women with PCOS and is associated with ovulatory dysfunction.
Glycated Serum Albumin and AGE Receptors.
Vetter, Fargo, United States. In Adv Clin Chem, 2014
In vivo modification of proteins by molecules with reactive carbonyl groups leads to intermediate and advanced glycation end products (AGE).
Immune and inflammatory mechanisms of atherosclerosis (*).
Ley et al., Norfolk, United States. In Annu Rev Immunol, 2008
Under proatherogenic conditions, nitric oxide production from endothelial cells is reduced and the burden of reactive oxygen species (ROS) and advanced glycation end products (AGE) is increased.
Methylglyoxal comes of AGE.
Schmidt et al., New York City, United States. In Cell, 2006
The posttranslational modification of proteins by methylglyoxal, a highly reactive compound derived from glycolysis, may contribute to aging, diabetes, and other disorders.
GlcNAc 2-epimerase can serve a catabolic role in sialic acid metabolism.
Bertozzi et al., Berkeley, United States. In J Biol Chem, 2003
determination of catabolic role in sialic acid metabolism
Benfotiamine blocks three major pathways of hyperglycemic damage and prevents experimental diabetic retinopathy.
Brownlee et al., Mannheim, Germany. In Nat Med, 2003
Three of the major biochemical pathways implicated in the pathogenesis of hyperglycemia induced vascular damage (the hexosamine pathway, the advanced glycation end product (AGE) formation pathway and the diacylglycerol (DAG)-protein kinase C (PKC) pathway) are activated by increased availability of the glycolytic metabolites glyceraldehyde-3-phosphate and fructose-6-phosphate.
Selective activation of N-acyl-D-glucosamine 2-epimerase expression in failing human heart ventricular myocytes.
Zisman et al., Albany, United States. In J Card Fail, 2003
gene and protein expression were selectively activated in left ventricular myocytes from end-stage failing human hearts
Identification of a domain conferring nucleotide binding to the N-acetyl-d-glucosamine 2-epimerase (Renin binding protein).
Mori et al., Akita, Japan. In J Biochem, 2002
domain structure of renin binding protein
Assignment of the gene encoding renin binding protein (Renbp) to rat chromosome Xq37 by in situ hybridization and radiation hybrid mapping.
Kreutz et al., Berlin, Germany. In Cytogenet Genome Res, 2001
The gene encoding renin binding protein (Renbp) has been assigned to rat chromosome Xq37.
Amino acid specificity of glycation and protein-AGE crosslinking reactivities determined with a dipeptide SPOT library.
Schinzel et al., Würzburg, Germany. In Nat Biotechnol, 1999
Advanced glycation end products (AGEs) contribute to changes in protein conformation, loss of function, and irreversible crosslinking.
RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides.
Schmidt et al., New York City, United States. In Cell, 1999
We report here that receptor for AGE (RAGE) is a central cell surface receptor for EN-RAGE (extracellular newly identified RAGE-binding protein) and related members of the S100/calgranulin superfamily.
share on facebooktweetadd +1mail to friends